Globular tail of myosin-V is bound to VAMP/synaptobrevin

被引:60
作者
Ohyama, A
Komiya, Y
Igarashi, M
机构
[1] Niigata Univ, Sch Med, Dept Biochem, Niigata 9518510, Japan
[2] Gunma Univ, Sch Med, Dept Anesthesiol & Reanimatol, Maebashi, Gumma 3718511, Japan
[3] Gunma Univ, Sch Med, Dept Mol & Cellular Neurobiol, Maebashi, Gumma 3718511, Japan
关键词
SNARE; myosin V; VAMP/synaptobrevin; syntaxin; calmodulin;
D O I
10.1006/bbrc.2001.4236
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
VAMP/synaptobrevin is one of a number of v-SNAREs involved in vesicular fusion events in neurons. In a previous report, VAMP was shown to form a complex with synaptophysin and myosin V, a motor protein based on the F-actin, and that myosin V was then released from the complex in a Ca2+-dependent manner. Here, we found that VAMP alone is bound to myosin V in a Ca2+-independent manner, and determined that the globular tail domain of myosin V is its binding site. The syntaxin-VAMP-myosin V formed in the presence of Ca2+/calmodulin (CaM), In the absence of CaM, only syntaxin-VAMP, or VAMP-myosin V complex was formed. Our results suggest that VAMP acts as a myosin V receptor on the vesicles and regulates formation of the complex. (C) 2001 Academic Press.
引用
收藏
页码:988 / 991
页数:4
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